Ferritin light chain: Difference between revisions

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  <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Ferritin light chain''' is a [[protein]] that in humans is encoded by the ''FTL'' [[gene]].<ref name="pmid3000916">{{cite journal | vauthors = Lebo RV, Kan YW, Cheung MC, Jain SK, Drysdale J | title = Human ferritin light chain gene sequences mapped to several sorted chromosomes | journal = Hum. Genet. | volume = 71 | issue = 4 | pages = 325–8 | date = December 1985 | pmid = 3000916 | pmc =  | doi = 10.1007/BF00388458 }}</ref><ref name="pmid9526618">{{cite journal | vauthors = Gasparini P, Calvano S, Memeo E, Bisceglia L, Zelante L | title = Assignment of ferritin L gene (FTL) to human chromosome band 19q13.3 by in situ hybridization | journal = Ann. Genet. | volume = 40 | issue = 4 | pages = 227–8 | year = 1997 | date = Apr 1997 | pmid = 9526618 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web |title=FTL ferritin, light polypeptide |url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2512 |publisher=[[National Center for Biotechnology Information]] |date=5 July 2009 |accessdate=20 July 2009}}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
It is abnormally expressed in fetuses of both [[in vitro fertilization|IVF]] and [[intracytoplasmic sperm injection|ICSI]], which may contribute to the increase risk of birth defects in these [[assisted reproductive technology|ART]].<ref name=zhang>{{cite journal | vauthors = Zhang Y, Zhang YL, Feng C, Wu YT, Liu AX, Sheng JZ, Cai J, Huang HF | title = Comparative proteomic analysis of human placenta derived from assisted reproductive technology | journal = Proteomics | volume = 8 | issue = 20 | pages = 4344–56 | date = October 2008 | pmid = 18792929 | doi = 10.1002/pmic.200800294 }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_FTL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ffx.
| PDB = {{PDB2|2ffx}}, {{PDB2|2fg4}}, {{PDB2|2fg8}}
| Name = Ferritin, light polypeptide
| HGNCid = 3999
| Symbol = FTL
| AltSymbols =; MGC71996
| OMIM = 134790
| ECnumber = 
| Homologene = 79330
| MGIid = 95590
| GeneAtlas_image1 = PBB_GE_FTL_212788_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_FTL_213187_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0008199 |text = ferric iron binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0008043 |text = ferritin complex}}
| Process = {{GNF_GO|id=GO:0006826 |text = iron ion transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2512
    | Hs_Ensembl = ENSG00000087086
    | Hs_RefseqProtein = NP_000137
    | Hs_RefseqmRNA = NM_000146
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 54160378
    | Hs_GenLoc_end = 54161850
    | Hs_Uniprot = P02792
    | Mm_EntrezGene = 14337
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_008049
    | Mm_RefseqProtein = NP_032075
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr =   
    | Mm_GenLoc_start =
    | Mm_GenLoc_end =
    | Mm_Uniprot =
  }}
}}
'''Ferritin, light polypeptide''', also known as '''FTL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FTL ferritin, light polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2512| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = This gene encodes the light subunit of the [[ferritin]] [[protein]]. Ferritin is the major intracellular iron storage protein in [[prokaryote]]s and [[eukaryote]]s. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyperferritinemia-cataract syndrome. This gene has multiple [[pseudogene]]s.<ref name="entrez">{{cite web | title = Entrez Gene: FTL ferritin, light polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2512| accessdate = }}</ref>
}}


==See also==
This gene encodes the light subunit of the [[ferritin]] [[protein]]. Ferritin is the major intracellular iron storage protein in [[prokaryote]]s and [[eukaryote]]s. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. This gene has multiple [[pseudogene]]s.<ref name="entrez"/>
 
Although ferritin light chain has no ferroxidase activity, the light chain may be responsible for the electron transfer across the ferritin protein cage.<ref name="pmid25348725">{{cite journal | vauthors = Carmona U, Li L, Zhang L, Knez M | title = Ferritin light-chain subunits: key elements for the electron transfer across the protein cage | journal = Chemical Communications | volume = 50 | issue = 97 | pages = 15358–15361 | year = 2014 | pmid = 25348725 | doi = 10.1039/c4cc07996e }}</ref>
 
== Clinical significance ==
 
Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and [[hyperferritinemia-cataract syndrome]].<ref name="pmid17643933">{{cite journal | vauthors = Zandman-Goddard G, Shoenfeld Y | title = Ferritin in autoimmune diseases | journal = Autoimmun Rev | volume = 6 | issue = 7 | pages = 457–63 | year = 2007 | pmid = 17643933 | doi = 10.1016/j.autrev.2007.01.016 | url = }}</ref>
 
Mutations of the FTL gene cause the rare adult-onset [[basal ganglia disease]] also known as [[neuroferritinopathy]]).<ref name="pmid21286947">{{cite journal | vauthors = Gregory A, Hayflick SJ | title = Genetics of neurodegeneration with brain iron accumulation | journal = Curr Neurol Neurosci Rep | volume = 11 | issue = 3 | pages = 254–61 | year = 2011 | pmid = 21286947 | doi = 10.1007/s11910-011-0181-3 }}</ref>
 
== Interactions ==
 
Ferritin light chain has been shown to [[Protein-protein interaction|interact]] with [[FTH1]].<ref name=pmid16189514>{{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8  | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}</ref><ref name=pmid16169070>{{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68  | date = Sep 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}</ref>
 
== See also ==
* [[Ferritin]]
* [[Ferritin]]


==References==
== References ==
{{reflist|2}}
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Munro HN, Aziz N, Leibold EA, Murray M, Rogers J, Vass JK, White K | title = The ferritin genes: structure, expression, and regulation | journal = Ann. N. Y. Acad. Sci. | volume = 526 | issue =  | pages = 113–23 | year = 1988 | pmid = 3291676 | doi = 10.1111/j.1749-6632.1988.tb55497.x }}
* {{cite journal | vauthors = Cazzola M, Skoda RC | title = Translational pathophysiology: a novel molecular mechanism of human disease | journal = Blood | volume = 95 | issue = 11 | pages = 3280–8  | date = June 2000 | pmid = 10828006 | doi =  }}
* {{cite journal | vauthors = Arosio P, Adelman TG, Drysdale JW | title = On ferritin heterogeneity. Further evidence for heteropolymers | journal = J. Biol. Chem. | volume = 253 | issue = 12 | pages = 4451–8  | date = June 1978 | pmid = 659425 | doi =  | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=659425 }}
* {{cite journal | vauthors = Gatti RA, Shaked R, Mohandas TK, Salser W | title = Human ferritin genes: chromosomal assignments and polymorphisms | journal = Am. J. Hum. Genet. | volume = 41 | issue = 4 | pages = 654–67  | date = October 1987 | pmid = 2821803 | pmc = 1684326 | doi =  }}
* {{cite journal | vauthors = Chou CC, Gatti RA, Fuller ML, Concannon P, Wong A, Chada S, Davis RC, Salser WA | title = Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro | journal = Mol. Cell. Biol. | volume = 6 | issue = 2 | pages = 566–73  | date = February 1986 | pmid = 3023856 | pmc = 367547 | doi =  10.1128/mcb.6.2.566| url = http://mcb.asm.org/cgi/pmidlookup?view=long&pmid=3023856 }}
* {{cite journal | vauthors = Santoro C, Marone M, Ferrone M, Costanzo F, Colombo M, Minganti C, Cortese R, Silengo L | title = Cloning of the gene coding for human L apoferritin | journal = Nucleic Acids Res. | volume = 14 | issue = 7 | pages = 2863–76  | date = April 1986 | pmid = 3754330 | pmc = 339708 | doi = 10.1093/nar/14.7.2863 }}
* {{cite journal | vauthors = Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW | title = Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones | journal = J. Biol. Chem. | volume = 260 | issue = 21 | pages = 11755–61  | date = September 1985 | pmid = 3840162 | doi =  | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3840162 }}
* {{cite journal | vauthors = Worwood M, Brook JD, Cragg SJ, Hellkuhl B, Jones BM, Perera P, Roberts SH, Shaw DJ | title = Assignment of human ferritin genes to chromosomes 11 and 19q13.3----19qter | journal = Hum. Genet. | volume = 69 | issue = 4 | pages = 371–4 | year = 1985 | pmid = 3857215 | doi = 10.1007/BF00291657 }}
* {{cite journal | vauthors = Dörner MH, Salfeld J, Will H, Leibold EA, Vass JK, Munro HN | title = Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 82 | issue = 10 | pages = 3139–43  | date = May 1985 | pmid = 3858810 | pmc = 397730 | doi = 10.1073/pnas.82.10.3139 }}
* {{cite journal | vauthors = Caskey JH, Jones C, Miller YE, Seligman PA | title = Human ferritin gene is assigned to chromosome 19 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 80 | issue = 2 | pages = 482–6  | date = January 1983 | pmid = 6572903 | pmc = 393402 | doi = 10.1073/pnas.80.2.482 }}
* {{cite journal | vauthors = Addison JM, Fitton JE, Lewis WG, May K, Harrison PM | title = The amino acid sequence of human liver apoferritin | journal = FEBS Lett. | volume = 164 | issue = 1 | pages = 139–44  | date = November 1983 | pmid = 6653779 | doi = 10.1016/0014-5793(83)80037-4 }}
* {{cite journal | vauthors = Girelli D, Corrocher R, Bisceglia L, Olivieri O, De Franceschi L, Zelante L, Gasparini P | title = Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: a mutation in the iron-responsive element of ferritin L-subunit gene (the "Verona mutation") | journal = Blood | volume = 86 | issue = 11 | pages = 4050–3  | date = December 1995 | pmid = 7492760 | doi =  | url = http://www.bloodjournal.org/cgi/pmidlookup?view=long&pmid=7492760 }}
* {{cite journal | vauthors = Beaumont C, Leneuve P, Devaux I, Scoazec JY, Berthier M, Loiseau MN, Grandchamp B, Bonneau D | title = Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract | journal = Nat. Genet. | volume = 11 | issue = 4 | pages = 444–6  | date = December 1995 | pmid = 7493028 | doi = 10.1038/ng1295-444 }}
* {{cite journal | vauthors = D'Agostino P, Faniello MC, Quaresima B, Bevilacqua MA, Tiano MT, Ammendola R, Cimino F, Costanzo F | title = Negative and positive elements in the promoter region of the human apoferritin L gene | journal = Biochem. Biophys. Res. Commun. | volume = 215 | issue = 1 | pages = 329–37  | date = October 1995 | pmid = 7575610 | doi = 10.1006/bbrc.1995.2470 }}
* {{cite journal | vauthors = Rogers JT, Andriotakis JL, Lacroix L, Durmowicz GP, Kasschau KD, Bridges KR | title = Translational enhancement of H-ferritin mRNA by interleukin-1 beta acts through 5' leader sequences distinct from the iron responsive element | journal = Nucleic Acids Res. | volume = 22 | issue = 13 | pages = 2678–86  | date = July 1994 | pmid = 8041631 | pmc = 308227 | doi = 10.1093/nar/22.13.2678 }}
* {{cite journal | vauthors = Spanner M, Weber K, Lanske B, Ihbe A, Siggelkow H, Schütze H, Atkinson MJ | title = The iron-binding protein ferritin is expressed in cells of the osteoblastic lineage in vitro and in vivo | journal = Bone | volume = 17 | issue = 2 | pages = 161–5  | date = August 1995 | pmid = 8554925 | doi = 10.1016/S8756-3282(95)00176-X }}
* {{cite journal | vauthors = Rogers JT | title = Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes | journal = Blood | volume = 87 | issue = 6 | pages = 2525–37  | date = March 1996 | pmid = 8630420 | doi =  | url = http://www.bloodjournal.org/cgi/pmidlookup?view=long&pmid=8630420 }}
* {{cite journal | vauthors = Pang JH, Jiang MJ, Chen YL, Wang FW, Wang DL, Chu SH, Chau LY | title = Increased ferritin gene expression in atherosclerotic lesions | journal = J. Clin. Invest. | volume = 97 | issue = 10 | pages = 2204–12  | date = May 1996 | pmid = 8636399 | pmc = 507299 | doi = 10.1172/JCI118661 }}
{{Refend}}
 
== External links ==
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=neuroferritin  GeneReviews/NCBI/NIH/UW entry on Neuroferritinopathy]
 
{{PDB Gallery|geneid=2512}}
 


==Further reading==
{{Molecular-cell-biology-stub}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Munro HN, Aziz N, Leibold EA, ''et al.'' |title=The ferritin genes: structure, expression, and regulation. |journal=Ann. N. Y. Acad. Sci. |volume=526 |issue=  |pages= 113-23 |year= 1988 |pmid= 3291676 |doi=  }}
*{{cite journal  | author=Cazzola M, Skoda RC |title=Translational pathophysiology: a novel molecular mechanism of human disease. |journal=Blood |volume=95 |issue= 11 |pages= 3280-8 |year= 2000 |pmid= 10828006 |doi=  }}
*{{cite journal  | author=Arosio P, Adelman TG, Drysdale JW |title=On ferritin heterogeneity. Further evidence for heteropolymers. |journal=J. Biol. Chem. |volume=253 |issue= 12 |pages= 4451-8 |year= 1978 |pmid= 659425 |doi=  }}
*{{cite journal  | author=Gatti RA, Shaked R, Mohandas TK, Salser W |title=Human ferritin genes: chromosomal assignments and polymorphisms. |journal=Am. J. Hum. Genet. |volume=41 |issue= 4 |pages= 654-67 |year= 1987 |pmid= 2821803 |doi=  }}
*{{cite journal  | author=Lebo RV, Kan YW, Cheung MC, ''et al.'' |title=Human ferritin light chain gene sequences mapped to several sorted chromosomes. |journal=Hum. Genet. |volume=71 |issue= 4 |pages= 325-8 |year= 1986 |pmid= 3000916 |doi=  }}
*{{cite journal  | author=Chou CC, Gatti RA, Fuller ML, ''et al.'' |title=Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. |journal=Mol. Cell. Biol. |volume=6 |issue= 2 |pages= 566-73 |year= 1987 |pmid= 3023856 |doi=  }}
*{{cite journal  | author=Santoro C, Marone M, Ferrone M, ''et al.'' |title=Cloning of the gene coding for human L apoferritin. |journal=Nucleic Acids Res. |volume=14 |issue= 7 |pages= 2863-76 |year= 1986 |pmid= 3754330 |doi=  }}
*{{cite journal  | author=Boyd D, Vecoli C, Belcher DM, ''et al.'' |title=Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. |journal=J. Biol. Chem. |volume=260 |issue= 21 |pages= 11755-61 |year= 1985 |pmid= 3840162 |doi=  }}
*{{cite journal  | author=Worwood M, Brook JD, Cragg SJ, ''et al.'' |title=Assignment of human ferritin genes to chromosomes 11 and 19q13.3----19qter. |journal=Hum. Genet. |volume=69 |issue= 4 |pages= 371-4 |year= 1985 |pmid= 3857215 |doi=  }}
*{{cite journal  | author=Dörner MH, Salfeld J, Will H, ''et al.'' |title=Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 10 |pages= 3139-43 |year= 1985 |pmid= 3858810 |doi=  }}
*{{cite journal  | author=Caskey JH, Jones C, Miller YE, Seligman PA |title=Human ferritin gene is assigned to chromosome 19. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 2 |pages= 482-6 |year= 1983 |pmid= 6572903 |doi=  }}
*{{cite journal  | author=Addison JM, Fitton JE, Lewis WG, ''et al.'' |title=The amino acid sequence of human liver apoferritin. |journal=FEBS Lett. |volume=164 |issue= 1 |pages= 139-44 |year= 1984 |pmid= 6653779 |doi=  }}
*{{cite journal  | author=Girelli D, Corrocher R, Bisceglia L, ''et al.'' |title=Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: a mutation in the iron-responsive element of ferritin L-subunit gene (the "Verona mutation") |journal=Blood |volume=86 |issue= 11 |pages= 4050-3 |year= 1996 |pmid= 7492760 |doi=  }}
*{{cite journal  | author=Beaumont C, Leneuve P, Devaux I, ''et al.'' |title=Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 444-6 |year= 1996 |pmid= 7493028 |doi= 10.1038/ng1295-444 }}
*{{cite journal  | author=D'Agostino P, Faniello MC, Quaresima B, ''et al.'' |title=Negative and positive elements in the promoter region of the human apoferritin L gene. |journal=Biochem. Biophys. Res. Commun. |volume=215 |issue= 1 |pages= 329-37 |year= 1995 |pmid= 7575610 |doi=  }}
*{{cite journal  | author=Rogers JT, Andriotakis JL, Lacroix L, ''et al.'' |title=Translational enhancement of H-ferritin mRNA by interleukin-1 beta acts through 5' leader sequences distinct from the iron responsive element. |journal=Nucleic Acids Res. |volume=22 |issue= 13 |pages= 2678-86 |year= 1994 |pmid= 8041631 |doi=  }}
*{{cite journal  | author=Spanner M, Weber K, Lanske B, ''et al.'' |title=The iron-binding protein ferritin is expressed in cells of the osteoblastic lineage in vitro and in vivo. |journal=Bone |volume=17 |issue= 2 |pages= 161-5 |year= 1996 |pmid= 8554925 |doi=  }}
*{{cite journal  | author=Rogers JT |title=Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes. |journal=Blood |volume=87 |issue= 6 |pages= 2525-37 |year= 1996 |pmid= 8630420 |doi=  }}
*{{cite journal  | author=Pang JH, Jiang MJ, Chen YL, ''et al.'' |title=Increased ferritin gene expression in atherosclerotic lesions. |journal=J. Clin. Invest. |volume=97 |issue= 10 |pages= 2204-12 |year= 1996 |pmid= 8636399 |doi=  }}
}}
{{refend}}
{{WikiDoc Sources}}

Latest revision as of 11:30, 30 November 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ferritin light chain is a protein that in humans is encoded by the FTL gene.[1][2][3]

It is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increase risk of birth defects in these ART.[4]

Function

This gene encodes the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. This gene has multiple pseudogenes.[3]

Although ferritin light chain has no ferroxidase activity, the light chain may be responsible for the electron transfer across the ferritin protein cage.[5]

Clinical significance

Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyperferritinemia-cataract syndrome.[6]

Mutations of the FTL gene cause the rare adult-onset basal ganglia disease also known as neuroferritinopathy).[7]

Interactions

Ferritin light chain has been shown to interact with FTH1.[8][9]

See also

References

  1. ↑ Lebo RV, Kan YW, Cheung MC, Jain SK, Drysdale J (December 1985). "Human ferritin light chain gene sequences mapped to several sorted chromosomes". Hum. Genet. 71 (4): 325–8. doi:10.1007/BF00388458. PMID 3000916.
  2. ↑ Gasparini P, Calvano S, Memeo E, Bisceglia L, Zelante L (Apr 1997). "Assignment of ferritin L gene (FTL) to human chromosome band 19q13.3 by in situ hybridization". Ann. Genet. 40 (4): 227–8. PMID 9526618.
  3. ↑ 3.0 3.1 "FTL ferritin, light polypeptide". National Center for Biotechnology Information. 5 July 2009. Retrieved 20 July 2009.
  4. ↑ Zhang Y, Zhang YL, Feng C, Wu YT, Liu AX, Sheng JZ, Cai J, Huang HF (October 2008). "Comparative proteomic analysis of human placenta derived from assisted reproductive technology". Proteomics. 8 (20): 4344–56. doi:10.1002/pmic.200800294. PMID 18792929.
  5. ↑ Carmona U, Li L, Zhang L, Knez M (2014). "Ferritin light-chain subunits: key elements for the electron transfer across the protein cage". Chemical Communications. 50 (97): 15358–15361. doi:10.1039/c4cc07996e. PMID 25348725.
  6. ↑ Zandman-Goddard G, Shoenfeld Y (2007). "Ferritin in autoimmune diseases". Autoimmun Rev. 6 (7): 457–63. doi:10.1016/j.autrev.2007.01.016. PMID 17643933.
  7. ↑ Gregory A, Hayflick SJ (2011). "Genetics of neurodegeneration with brain iron accumulation". Curr Neurol Neurosci Rep. 11 (3): 254–61. doi:10.1007/s11910-011-0181-3. PMID 21286947.
  8. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  9. ↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.

Further reading

External links


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